메뉴 건너뛰기




Volumn 338, Issue 1, 2005, Pages 365-371

Subzero-temperature stabilization and spectroscopic characterization of homogeneous oxyferrous complexes of the cytochrome P450 BM3 (CYP102) oxygenase domain and holoenzyme

Author keywords

Cryoenzymology; Cysteinate ligated heme iron; Cytochrome P450 BM3; Dioxygen activation; Magnetic circular dichroism; Mono oxygenase; Oxyferrous heme iron

Indexed keywords

CYTOCHROME P450; CYTOCHROME P450 BM3; HEMOPROTEIN; HOLOENZYME; OXYGENASE; QUERCETIN; UNCLASSIFIED DRUG;

EID: 27544513115     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2005.08.078     Document Type: Article
Times cited : (11)

References (26)
  • 1
    • 0034973773 scopus 로고    scopus 로고
    • Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity
    • F.P. Guengerich Common and uncommon cytochrome P450 reactions related to metabolism and chemical toxicity Chem. Res. Toxicol. 14 2001 611 650
    • (2001) Chem. Res. Toxicol. , vol.14 , pp. 611-650
    • Guengerich, F.P.1
  • 2
    • 0035984571 scopus 로고    scopus 로고
    • Oxidizing species in the mechanism of cytochrome P450
    • P.R. Ortiz de Montellano, and J.J. De Voss Oxidizing species in the mechanism of cytochrome P450 Nat. Prod. Rep. 19 2002 477 493
    • (2002) Nat. Prod. Rep. , vol.19 , pp. 477-493
    • Ortiz De Montellano, P.R.1    De Voss, J.J.2
  • 4
    • 13444266016 scopus 로고    scopus 로고
    • Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy
    • R. Davydov, R. Perera, S. Jin, T.C. Yang, T.A. Bryson, M. Sono, J.H. Dawson, and B.M. Hoffman Substrate modulation of the properties and reactivity of the oxy-ferrous and hydroperoxo-ferric intermediates of cytochrome P450cam as shown by cryoreduction-EPR/ENDOR spectroscopy J. Am. Chem. Soc. 127 2005 1403 1413
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 1403-1413
    • Davydov, R.1    Perera, R.2    Jin, S.3    Yang, T.C.4    Bryson, T.A.5    Sono, M.6    Dawson, J.H.7    Hoffman, B.M.8
  • 5
    • 0033579110 scopus 로고    scopus 로고
    • EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: Mutation-induced changes in the proton delivery system
    • R. Davydov, I.D. Macdonald, T.M. Makris, S.G. Sligar, and B.M. Hoffman EPR and ENDOR of catalytic intermediates in cryoreduced native and mutant oxy-cytochromes P450cam: mutation-induced changes in the proton delivery system J. Am. Chem. Soc. 121 1999 10654 10655
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 10654-10655
    • Davydov, R.1    MacDonald, I.D.2    Makris, T.M.3    Sligar, S.G.4    Hoffman, B.M.5
  • 6
    • 0027375275 scopus 로고
    • Molecular recognition in cytochrome P-450: Mechanism for the control of uncoupling reactions
    • P.J. Loida, and S.G. Sligar Molecular recognition in cytochrome P-450: mechanism for the control of uncoupling reactions Biochemistry 32 1993 11530 11538
    • (1993) Biochemistry , vol.32 , pp. 11530-11538
    • Loida, P.J.1    Sligar, S.G.2
  • 7
    • 0347927627 scopus 로고    scopus 로고
    • Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus
    • J.K. Yano, F. Blasco, H. Li, R.D. Schmid, A. Henne, and T.J. Poulos Preliminary characterization and crystal structure of a thermostable cytochrome P450 from Thermus thermophilus J. Biol. Chem. 278 2003 608 616
    • (2003) J. Biol. Chem. , vol.278 , pp. 608-616
    • Yano, J.K.1    Blasco, F.2    Li, H.3    Schmid, R.D.4    Henne, A.5    Poulos, T.J.6
  • 8
    • 0029137990 scopus 로고
    • Modeling protein-substrate interactions in the heme domain of cytochrome P450(BM-3)
    • H. Li, and T.L. Poulos Modeling protein-substrate interactions in the heme domain of cytochrome P450(BM-3) Acta Crystallogr. D51 1995 21 32
    • (1995) Acta Crystallogr. , vol.51 , pp. 21-32
    • Li, H.1    Poulos, T.L.2
  • 9
    • 0028898244 scopus 로고
    • Reaction of carbon monoxide and molecular oxygen with P450terp (CYP108) and P450BM-3 (CYP102)
    • I.F. Sevrioukova, and J.A. Peterson Reaction of carbon monoxide and molecular oxygen with P450terp (CYP108) and P450BM-3 (CYP102) Arch. Biochem. Biophys. 317 1995 397 404
    • (1995) Arch. Biochem. Biophys. , vol.317 , pp. 397-404
    • Sevrioukova, I.F.1    Peterson, J.A.2
  • 11
    • 14744296960 scopus 로고    scopus 로고
    • The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM
    • M. Sono, R. Perera, S. Jin, T.M. Makris, S.G. Sligar, T.A. Bryson, and J.H. Dawson The influence of substrate on the spectral properties of oxyferrous wild-type and T252A cytochrome P450-CAM Arch. Biochem. Biophys. 436 2005 40 49
    • (2005) Arch. Biochem. Biophys. , vol.436 , pp. 40-49
    • Sono, M.1    Perera, R.2    Jin, S.3    Makris, T.M.4    Sligar, S.G.5    Bryson, T.A.6    Dawson, J.H.7
  • 12
    • 0030014679 scopus 로고    scopus 로고
    • The flavoprotein domain of P450BM-3: Expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomain
    • I. Sevrioukova, G. Truan, and J.A. Peterson The flavoprotein domain of P450BM-3: expression, purification, and properties of the flavin adenine dinucleotide- and flavin mononucleotide-binding subdomain Biochemistry 35 1996 7528 7535
    • (1996) Biochemistry , vol.35 , pp. 7528-7535
    • Sevrioukova, I.1    Truan, G.2    Peterson, J.A.3
  • 13
    • 0030960888 scopus 로고    scopus 로고
    • The domain architecture of cytochrome P450BM-3
    • S. Govindaraj, and T.L. Poulos The domain architecture of cytochrome P450BM-3 J. Biol. Chem. 272 1997 7915 7921
    • (1997) J. Biol. Chem. , vol.272 , pp. 7915-7921
    • Govindaraj, S.1    Poulos, T.L.2
  • 14
    • 0037199484 scopus 로고    scopus 로고
    • Regioselective peroxo-dependent heme alkylation in P450BM3-F87G by aromatic aldehydes: Effects of alkylation on catalysis
    • G.M. Raner, J.A. Hatchell, M.U. Dixon, T.L. Joy, A.E. Haddy, and E.R. Johnston Regioselective peroxo-dependent heme alkylation in P450BM3-F87G by aromatic aldehydes: effects of alkylation on catalysis Biochemistry 41 2002 9601 9610
    • (2002) Biochemistry , vol.41 , pp. 9601-9610
    • Raner, G.M.1    Hatchell, J.A.2    Dixon, M.U.3    Joy, T.L.4    Haddy, A.E.5    Johnston, E.R.6
  • 15
    • 0027522735 scopus 로고
    • Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3
    • M.L. Klein, and A.J. Fulco Critical residues involved in FMN binding and catalytic activity in cytochrome P450BM-3 J. Biol. Chem. 268 1993 7553 7561
    • (1993) J. Biol. Chem. , vol.268 , pp. 7553-7561
    • Klein, M.L.1    Fulco, A.J.2
  • 16
    • 0000982535 scopus 로고
    • Imidazole- and alkylamine-ligated iron(II,III) chlorin complexes as models for histidine and lysine coordination to iron in dihydroporphyrin- containing proteins: Characterization with magnetic circular dichroism spectroscopy
    • A.M. Huff, C.K. Chang, D.K. Cooper, K.M. Smith, and J.H. Dawson Imidazole- and alkylamine-ligated iron(II,III) chlorin complexes as models for histidine and lysine coordination to iron in dihydroporphyrin-containing proteins: characterization with magnetic circular dichroism spectroscopy Inorg. Chem. 32 1993 1460 1466
    • (1993) Inorg. Chem. , vol.32 , pp. 1460-1466
    • Huff, A.M.1    Chang, C.K.2    Cooper, D.K.3    Smith, K.M.4    Dawson, J.H.5
  • 19
    • 2542520761 scopus 로고    scopus 로고
    • Theoretical study of the ligand-CYP2B4 complexes: Effect of structure on binding free energies and heme spin state
    • D.L. Harris, J. Park, L. Gruenke, and L. Waskell Theoretical study of the ligand-CYP2B4 complexes: effect of structure on binding free energies and heme spin state Proteins 55 2004 895 914
    • (2004) Proteins , vol.55 , pp. 895-914
    • Harris, D.L.1    Park, J.2    Gruenke, L.3    Waskell, L.4
  • 20
    • 0033616081 scopus 로고    scopus 로고
    • The role of the distal and proximal protein environments in controlling the ferric spin state and in stabilizing thiolate ligation in heme systems
    • M.P. Roach, A.E. Pond, M.R. Thomas, S.G. Boxer, and J.H. Dawson The role of the distal and proximal protein environments in controlling the ferric spin state and in stabilizing thiolate ligation in heme systems J. Am. Chem. Soc. 121 1999 12088 12093
    • (1999) J. Am. Chem. Soc. , vol.121 , pp. 12088-12093
    • Roach, M.P.1    Pond, A.E.2    Thomas, M.R.3    Boxer, S.G.4    Dawson, J.H.5
  • 21
    • 0033619706 scopus 로고    scopus 로고
    • Essential thiol requirement to restore pterin- or substrate-binding capability and to regenerate native enzyme-type high-spin heme spectra in the Escherichia coli-expressed tetrahydrobiopterin-free oxygenase domain of neuronal nitric oxide synthase
    • M. Sono, A.P. Ledbetter, K. McMillan, L.J. Roman, T.M. Shea, B.S.S. Masters, and J.H. Dawson Essential thiol requirement to restore pterin- or substrate-binding capability and to regenerate native enzyme-type high-spin heme spectra in the Escherichia coli-expressed tetrahydrobiopterin-free oxygenase domain of neuronal nitric oxide synthase Biochemistry 38 1999 15853 15862
    • (1999) Biochemistry , vol.38 , pp. 15853-15862
    • Sono, M.1    Ledbetter, A.P.2    McMillan, K.3    Roman, L.J.4    Shea, T.M.5    Masters, B.S.S.6    Dawson, J.H.7
  • 23
    • 0016184960 scopus 로고
    • A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes
    • W.J. Wallace, J.C. Maxwell, and W.S. Caughey A role for chloride in the autoxidation of hemoglobin under conditions similar to those in erythrocytes FEBS Lett. 43 1974 33 36
    • (1974) FEBS Lett. , vol.43 , pp. 33-36
    • Wallace, W.J.1    Maxwell, J.C.2    Caughey, W.S.3
  • 24
    • 0016156128 scopus 로고
    • The mechanism of hemoglobin autoxidation evidence for proton-assisted nucleophilic displacement of superoxide by anions
    • W.J. Wallace, J.C. Maxwell, and W.S. Caughey The mechanism of hemoglobin autoxidation evidence for proton-assisted nucleophilic displacement of superoxide by anions Biochem. Biophys. Res. Commun. 57 1974 1104 1110
    • (1974) Biochem. Biophys. Res. Commun. , vol.57 , pp. 1104-1110
    • Wallace, W.J.1    Maxwell, J.C.2    Caughey, W.S.3
  • 25
    • 0017302087 scopus 로고
    • Oxidized cytochrome P450. MCD evidence for thiolate ligation in the substrate-bound form. Implication for the catalytic mechanism
    • J.H. Dawson, R.H. Holm, J.R. Trudell, G. Barth, R.E. Linder, E. Bunnenberg, C. Djerassi, and S.C. Tang Oxidized cytochrome P450. MCD evidence for thiolate ligation in the substrate-bound form. Implication for the catalytic mechanism J. Am. Chem. Soc. 98 1976 3707
    • (1976) J. Am. Chem. Soc. , vol.98 , pp. 3707
    • Dawson, J.H.1    Holm, R.H.2    Trudell, J.R.3    Barth, G.4    Linder, R.E.5    Bunnenberg, E.6    Djerassi, C.7    Tang, S.C.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.